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Accession number;06A0759487
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| Title;Crystal Structure of Ca'2+'-dependent Lectin from a Marine Invertebrate and its Hemolytic Mechanisms |
| Author;
UCHIDA TATSUYA
(Inst. for Protein Res., Osaka Univ.)
HATAKEYAMA TOMOMITSU
(Nagasaki Univ., Fac. of Eng.)
KUSUNOKI MASAMI
(Inst. for Protein Res., Osaka Univ.)
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Journal Title;Journal of the Crystallographic Society of Japan
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Journal Code:G0232A
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ISSN:0369-4585
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VOL.48;NO.4;PAGE.290-295(2006)
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| Figure&Table&Reference;FIG.5, TBL.2, REF.15 |
| Pub. Country;Japan |
| Language;Japanese |
| Abstract;CEL-III is a Ca'2+'-dependent animal lectin from the sea cucumber, Cucumaria echinata, which shows binding specificity for galactose-containing carbohydrates and exhibits hemolytic and hemagglutinating activities. We have determined its crystal structure at 1.7.ANGS. resolution by using single isomorphous replacement with anomalous scattering of lead. CEL-III consists of N-terminal two carbohydrate-binding domains and a C-terminal domain, which is essential for oligomerization and binding to a membrane. CEL-III is the first structure with two .BETA.-trefoil folds containing five Ca'2+' ions. Here, we report the structural features of CEL-III and discuss the mechanisms of recognition of carbohydrates and hemolysis. (author abst.) |
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